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Gene Review

ERI1  -  Eri1p

Saccharomyces cerevisiae S288c

Synonyms: Endoplasmic reticulum-associated Ras inhibitor protein 1, Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit, RIN1, YPL096C-A
 
 
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High impact information on ERI1

  • The yeast ERI1 gene encodes a small ER-localized protein that associates in vivo with GTP bound Ras2 in an effector loop-dependent manner [1].
  • We showed previously that loss of Eri1 function results in hyperactive Ras phenotypes [1].
  • Here, we demonstrate that Eri1 is a component of the GPI-GlcNAc transferase (GPI-GnT) complex in the ER, which catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI-anchors for cell surface proteins [1].
  • A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum [2].
  • ERI1 encodes a 68-amino-acid protein that associates in vivo with GTP-bound Ras in a manner that requires an intact Ras-effector loop, suggesting that Eri1 competes for the same binding site as Ras target proteins [2].
 

Anatomical context of ERI1

  • Unlike Raf1, however, the Rin1 protein resides primarily at the plasma membrane, where H-Ras is localized [3].

References

  1. Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER. Sobering, A.K., Watanabe, R., Romeo, M.J., Yan, B.C., Specht, C.A., Orlean, P., Riezman, H., Levin, D.E. Cell (2004) [Pubmed]
  2. A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum. Sobering, A.K., Romeo, M.J., Vay, H.A., Levin, D.E. Mol. Cell. Biol. (2003) [Pubmed]
  3. A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1. Han, L., Colicelli, J. Mol. Cell. Biol. (1995) [Pubmed]
 
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